Structure of PDB 1ba0 Chain A

Receptor sequence
>1ba0A (length=378) Species: 9913 (Bos taurus) [Search protein sequence]
GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGD
AAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKV
QVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDS
QRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGG
TFKVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDI
SENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFE
ELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDF
FNGKELNKSINPDEAVAYGAAVQAAILS
3D structure
PDB1ba0 Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D10 K71 E175 D199
Catalytic site (residue number reindexed from 1) D7 K68 E172 D196
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP A T14 Y15 G201 G202 E268 K271 R272 S275 G338 G339 R342 D366 T11 Y12 G198 G199 E265 K268 R269 S272 G335 G336 R339 D363
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:1ba0, PDBe:1ba0, PDBj:1ba0
PDBsum1ba0
PubMed9585559
UniProtP19120|HSP7C_BOVIN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

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